ID A0A248TGW5_9BACI Unreviewed; 475 AA.
AC A0A248TGW5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146, ECO:0000256|RuleBase:RU362017};
DE Short=Aspartase {ECO:0000256|RuleBase:RU362017};
DE EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992, ECO:0000256|RuleBase:RU362017};
GN Name=aspA {ECO:0000313|EMBL:ASV67433.1};
GN ORFNames=CKF48_08885 {ECO:0000313|EMBL:ASV67433.1};
OS Cytobacillus kochii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=859143 {ECO:0000313|EMBL:ASV67433.1, ECO:0000313|Proteomes:UP000215137};
RN [1] {ECO:0000313|EMBL:ASV67433.1, ECO:0000313|Proteomes:UP000215137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDGP4 {ECO:0000313|EMBL:ASV67433.1,
RC ECO:0000313|Proteomes:UP000215137};
RA Wan K.H., Yu C., Park S., Hammonds A.S., Booth B.W., Celniker S.E.;
RT "Complete Genome Sequence of Bacillus kochii Oregon-R-modENCODE STRAIN
RT BDGP4, isolated from Drosophila melanogaster gut.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001494,
CC ECO:0000256|RuleBase:RU362017};
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596,
CC ECO:0000256|RuleBase:RU362017}.
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DR EMBL; CP022983; ASV67433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248TGW5; -.
DR KEGG; bko:CKF48_08885; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000215137; Chromosome.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd01357; Aspartase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR InterPro; IPR004708; ApsA.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR018951; Fumarase_C_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00839; aspA; 1.
DR PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1.
DR PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017};
KW Reference proteome {ECO:0000313|Proteomes:UP000215137}.
FT DOMAIN 15..344
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 410..463
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 475 AA; 52149 MW; B782F9D7EAA08801 CRC64;
MSNDKVRIEN DFLGSKEVPI DAYYGVQTLR AVENFPITGY RIHEELIIAI AMVKKAAALA
NMDTKRLYEG LGNVIVQAAD EIIEGKWHDH FIVDPIQGGA GTSINMNANE VIANRALELL
GKNKGDYALH LSPNSHVNMS QSTNDAFPTA IHIATLNALE KLTQTMEHML AAFKEKAKQF
DHVIKMGRTH LQDAVPIRLG QEFEAYSRVV TRDIKRIQQS RQHLYEINMG ATAVGTGLNA
DPIYIESVVK HMAEITGLPL VGADHLVDAT QNTDAYTEVS AALKVCMMNM SKIANDIRLM
ASGPRAGLGE ISLPARQPGS SIMPGKVNPV MPEMINQVAF QVIGNDHTIC LASEAGQLEL
NVMEPVLVFN LLQSISIMNN AFRAFTDYCL SGIEANETRL KEYVENSAGI ITAVNPHIGY
EVAARIAREA IINGKSVREL CLKYDVLTEE ELDLILNPYE MTNPGIAGVS LLNRD
//
